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| '''Heme Oxygenase''' (HO) is a member of the Hemoprotein family and catalyzes the Oxygen-dependent cleavage of the porphyrin ring of heme, using reducing equivalents like NADH to produce biliverdin, iron and CO <ref name="HO">PMID:17253780</ref>. HO consists of two main isoforms which are present in mammals, HO-1 and HO-2. The two isoforms are products of different genes, are different molecular sizes (32 kDa and 36 kDa respectively) and contain a different primary structure showing only 58% homology <ref name="HO1">PMID:15522396</ref>. However studies have shown that the two isoforms share a region with 100% secondary structure homology which is believed to be the catalytic site of the protein<ref name="HO"/>. The heme oxygenase isoforms are not free throughout the body but sequestered to certain tissues. The Heme oxygenase -1 is strongly expressed in the spleen and liver whereas Heme Oxygenase-2 is strongly expressed in the brain, testis and vascular systems<ref name="sc1">PMID:12909459</ref>. | | '''Heme Oxygenase''' (HO) is a member of the [[Hemeproteins|Hemoprotein family]] and catalyzes the Oxygen-dependent cleavage of the porphyrin ring of heme, using reducing equivalents like NADH to produce biliverdin, iron and CO <ref name="HO">PMID:17253780</ref>. HO consists of two main isoforms which are present in mammals, HO-1 and HO-2. The two isoforms are products of different genes, are different molecular sizes (32 kDa and 36 kDa respectively) and contain a different primary structure showing only 58% homology <ref name="HO1">PMID:15522396</ref>. However studies have shown that the two isoforms share a region with 100% secondary structure homology which is believed to be the catalytic site of the protein<ref name="HO"/>. The heme oxygenase isoforms are not free throughout the body but sequestered to certain tissues. |
| | *'''Heme oxygenase -1''' is inducible and is strongly expressed in the spleen and liver. |
| | *'''Heme Oxygenase-2''' is expressed constitutively and is strongly expressed in the brain, testis and vascular systems<ref name="sc1">PMID:12909459</ref>. |
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| ==='''Ligand'''=== | | ==='''Ligand'''=== |
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| ==Additional Resources== | | ==Additional Resources== |
| For additional information, See: [[Cancer]] <br /> | | For additional information, see: |
| For additional information, See: [[NADPH Cytochrome P450 Oxidoreductase]] <br />
| | *[[Cancer]] |
| </StructureSection>
| | *[[NADPH Cytochrome P450 Oxidoreductase]] |
| | *[[Hemeproteins]] |
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| ==3D structures of heme oxygenase== | | ==3D structures of heme oxygenase== |
| | [[Heme oxygenase 3D structures]] |
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| Updated on {{REVISIONDAY2}}-{{MONTHNAME|{{REVISIONMONTH}}}}-{{REVISIONYEAR}}
| | </StructureSection> |
| {{#tree:id=OrganizedByTopic|openlevels=0|
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| *Heme oxygenase
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| **[[2z68]], [[1wzd]], [[1wzf]], [[1wzg]], [[1iw0]], [[1iw1]], [[4goh]] – CdHO – ''Coreynebacterium diphtheriae''<BR />
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| **[[1wnv]], [[1wnw]], [[1wnx]] – CdHO (mutant) <BR />
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| **[[1ubb]], [[1dve]], [[1dvg]] – rHO – rat<BR />
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| **[[1irm]] – rHO-apo<BR />
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| **[[4mec]] – rHO-1 Zn containing<br />
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| **[[3gas]] – HO – ''Helicobacter pylori''<BR />
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| **[[1xk1]], [[1xk0]], [[1xjz]], [[1xk2]], [[1oyk]], [[1oyl]], [[1oze]], [[1ozr]], [[4wd4]] - hHO-1 (mutant) – human<BR />
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| **[[1n45]], [[1n3u]] – hHO-1<BR />
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| **[[1we1]] – HO-1 – ''Cyanobacterium synechocystis''<BR />
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| **[[1p3t]], [[1j77]] – NmHO-1 – ''Nisseria meningitides''<br />
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| **[[5kzl]] – HO (mutant) – ''Leptospira interrogans''<br />
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| *Heme oxygenase complex with NO
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| **[[1j02]] - rHO-1 + NO<BR />
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| **[[1kx3]], [[1ozl]], [[1ozw]], [[1xk3]] - hHO-1 (mutant) + NO<BR />
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| **[[1p3u]] - NmHO-1 + NO<BR />
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| *Heme oxygenase with verdoheme
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| **[[3moo]] – CdHO + verdoheme-N3<BR />
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| **[[2zvu]] – rHO-1 + verdoheme<BR />
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| **[[1twn]] - hHO-1 + verdoheme<BR />
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| **[[1twr]] - hHO-1 + verdoheme-NO<BR />
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| *Heme oxygenase complex with reaction products
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| **[[1p3v]] - NmHO-1 + CO<BR />
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| **[[1ulx]], [[1ix4]] - rHO-1 + CO<BR />
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| **[[1j2c]] - rHO-1 + biliverdine<BR />
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| **[[1s8c]] - hHO-1 + biliverdine<br />
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| **[[5btq]] – hHO-1 (mutant) + biliverdine<br />
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| **[[4gpc]], [[4gpf]], [[4gph]] - CdHO + biliverdine<br />
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| *Heme oxygenase binary complexes
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| **[[3i8r]], [[3i9t]] – CdHO + DTT<BR />
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| **[[1v8x]] – CdHO + O2<BR />
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| **[[4g7l]] – rHO-1 + O2<br />
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| **[[4g7p]], [[4g7t]], [[4g7u]], [[4g8p]], [[4g8u]], [[4g8w]], [[4g98]], [[4g99]] – rHO-1 + CO<br />
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| **[[3i9u]] – rHO-1 + DTE <BR />
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| **[[2e7e]], [[1ix3]] – rHO-1 + CN<BR />
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| **[[1ivj]] - rHO-1 + N3>br />
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| **[[1vgi]] - rHO-1 + Xe<BR />
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| **[[2dy5]] - rHO-1 + azole derivative<BR />
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| **[[3k4f]], [[3hok]], [[3czy]], [[3tgm]] – hHO-1 + azole derivative<BR />
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| **[[1ni6]] – hHO-1 + trehalose<BR />
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| **[[1s13]] - hHO-1 + 2-phenylheme<BR />
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| **[[1t5p]] - hHO-1 + 12-phenylheme<br />
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| **[[2zdo]] – SaHO + hemin – ''Staphylococcus aureus''<br />
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| **[[2zdp]] – SaHO + Co<br />
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| **[[3lgm]], [[3lgn]], [[3qgp]], [[4fnh]] – SaHO + heme<br />
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| **[[4fni]] – SaHO + heme + CN<br />
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| **[[3wkt]] – rHO-1 (mutant) + NADPH-cytochrome P450 reductase<br />
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| *Heme oxygenase 2
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| **[[5uc8]] – hHO-2<br />
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| **[[2rgz]], [[2qpp]], [[2q32]], [[4wmh]] – hHO-2 (mutant) <BR />
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| **[[5uc9]] – hHO-2 + myristate<br />
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| **[[5uca]] – hHO-2 + laurate<br />
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| **[[1wov]], [[1wow]] – SyHO-2 – ''Synechocystis''<BR />
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| **[[1wox]] – SyHO-2 + NO<BR />
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| **[[4raj]] – HO-2 – ''Chlamydominas reinhardtii''<br />
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| }}
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| ==References== | | ==References== |